CYP2D11 Inhibitors

CYP2D11, a member of the cytochrome P450 enzyme family, plays a crucial role in heme binding and monooxygenase activities. Its predicted involvement in arachidonic acid metabolic processes and xenobiotic metabolic processes, along with localization in the mitochondrion, underscores its significance in cellular homeostasis. Orthologous to CYP2D6, CYP2D11 is implicated in various diseases, including acute lymphoblastic leukemia, acute myeloid leukemia, asthma, autoimmune hepatitis, and rhinitis. The identification of CYP2D11 inhibitors reveals a diverse set of chemicals that may directly or indirectly modulate its activities. Quinidine directly inhibits CYP2D11 by interfering with monooxygenase activity, altering cytoplasmic dynamics and hindering the enzyme's predicted involvement in heme binding processes. Paroxetine, a selective serotonin reuptake inhibitor, acts as a direct inhibitor by suppressing monooxygenase activity, modifying mitochondrial and cytoplasmic dynamics, and hindering the enzyme's predicted participation in arachidonic acid metabolic processes.

Fluoxetine, another selective serotonin reuptake inhibitor, indirectly impacts CYP2D11 by suppressing monooxygenase activity and influencing intracellular membrane dynamics, hindering the enzyme's predicted involvement in arachidonic acid metabolic processes. Amiodarone directly inhibits CYP2D11 by interfering with monooxygenase activity, altering mitochondrial and cytoplasmic dynamics, and hindering the enzyme's predicted participation in xenobiotic metabolic processes. Bupropion, an atypical antidepressant, acts as a direct inhibitor of CYP2D11 by suppressing monooxygenase activity, modifying mitochondrial and intracellular membrane-bounded organelle functions, and hindering the enzyme's predicted involvement in xenobiotic metabolic processes. Sertraline, a selective serotonin reuptake inhibitor, directly inhibits CYP2D11 by suppressing monooxygenase activity, altering mitochondrial dynamics and intracellular membrane functions, and hindering the enzyme's predicted participation in arachidonic acid metabolic processes. Ritonavir acts as a direct inhibitor of CYP2D11 by interfering with monooxygenase activity, modifying mitochondrial and intracellular membrane-bounded organelle functions, and hindering the enzyme's predicted involvement in xenobiotic metabolic processes.